| pubmed-article:6741750 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6741750 | lifeskim:mentions | umls-concept:C0162807 | lld:lifeskim |
| pubmed-article:6741750 | lifeskim:mentions | umls-concept:C0017082 | lld:lifeskim |
| pubmed-article:6741750 | lifeskim:mentions | umls-concept:C0725066 | lld:lifeskim |
| pubmed-article:6741750 | lifeskim:mentions | umls-concept:C0205225 | lld:lifeskim |
| pubmed-article:6741750 | lifeskim:mentions | umls-concept:C0332185 | lld:lifeskim |
| pubmed-article:6741750 | lifeskim:mentions | umls-concept:C0204514 | lld:lifeskim |
| pubmed-article:6741750 | pubmed:dateCreated | 1984-8-23 | lld:pubmed |
| pubmed-article:6741750 | pubmed:abstractText | High-field (500 MHz) proton NMR has been used to elucidate the primary and secondary structures of glycosphingolipids (GSLs). Using 2-D J-correlated spectroscopy (2-D SECSY) which establishes scalar couplings of protons, the monosaccharide composition, anomeric configuration and aglycon structures of a GSL can be established. 2-D nuclear Overhauser effect spectroscopy (2-D NOE) then establishes through-space intra- and inter-residue couplings of cross-relaxing protons. We have found that each anomeric proton is involved in NOE couplings with inter- and intra-residue protons. The inter-residue coupling, resulting from interaction of protons across the glycosidic linkage, establishes the n-1 sugar residue and specific glycosidation site to which the n-residue is linked. When such information is known for each residue and is combined, the sequence of the core oligosaccharide is obtained. The sialylation-induced glycosidation shift is then used to establish the site of sialic acid residue attachment in a ganglioside molecule. We have also observed that the anomeric proton inter-residue NOE couplings can be used to suggest the preferred conformation of an oligosaccharide. We have found that the oligosaccharide residue of globoside exists in a unique and rather rigid conformation which could be stabilized by hydrogen bonds and van der Waals interactions. Since GSLs are known to have a receptor role and are implicated in cell-cell recognition, enzyme-substrate interaction and antigen-antibody interaction, the determination of their conformation should be useful in understanding their biological functions. | lld:pubmed |
| pubmed-article:6741750 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6741750 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6741750 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6741750 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6741750 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6741750 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6741750 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6741750 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6741750 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6741750 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6741750 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6741750 | pubmed:issn | 0065-2598 | lld:pubmed |
| pubmed-article:6741750 | pubmed:author | pubmed-author:YuR KRK | lld:pubmed |
| pubmed-article:6741750 | pubmed:author | pubmed-author:PrestegardJ... | lld:pubmed |
| pubmed-article:6741750 | pubmed:author | pubmed-author:KoernerT... | lld:pubmed |
| pubmed-article:6741750 | pubmed:author | pubmed-author:ScarsdaleJ... | lld:pubmed |
| pubmed-article:6741750 | pubmed:author | pubmed-author:DemosP APA | lld:pubmed |
| pubmed-article:6741750 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6741750 | pubmed:volume | 174 | lld:pubmed |
| pubmed-article:6741750 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6741750 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6741750 | pubmed:pagination | 87-102 | lld:pubmed |
| pubmed-article:6741750 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:6741750 | pubmed:meshHeading | pubmed-meshheading:6741750-... | lld:pubmed |
| pubmed-article:6741750 | pubmed:meshHeading | pubmed-meshheading:6741750-... | lld:pubmed |
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| pubmed-article:6741750 | pubmed:meshHeading | pubmed-meshheading:6741750-... | lld:pubmed |
| pubmed-article:6741750 | pubmed:meshHeading | pubmed-meshheading:6741750-... | lld:pubmed |
| pubmed-article:6741750 | pubmed:meshHeading | pubmed-meshheading:6741750-... | lld:pubmed |
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| pubmed-article:6741750 | pubmed:meshHeading | pubmed-meshheading:6741750-... | lld:pubmed |
| pubmed-article:6741750 | pubmed:year | 1984 | lld:pubmed |
| pubmed-article:6741750 | pubmed:articleTitle | Recent advances in structural analysis of gangliosides: primary and secondary structures. | lld:pubmed |
| pubmed-article:6741750 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6741750 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:6741750 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:6741750 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
